Valentina Caseli
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Valentina Caseli has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Alberto Boffi
Department of Biochemical Sciences—A. Rossi Fanelli, Sapienza University, 00185 Rome, Italy
1 shared publication - Alberto Macone
Department of Biochemical Science “A. Rossi Fanelli”, Faculty of Pharmacy and Medicine, Sapienza University of Rome, P.le Aldo Moro 5, 00185 Rome, Italy
1 shared publication - Alessandra Bonamore
Department of Biochemical Sciences—A. Rossi Fanelli, Sapienza University, 00185 Rome, Italy
1 shared publication - Alessio Incocciati
Department of Biochemical Sciences—A. Rossi Fanelli, Sapienza University, 00185 Rome, Italy
1 shared publication - Antonia Iazzetti
Dipartimento di Scienze Biotecnologiche di Base Cliniche Intensivologiche e Perioperatorie Università Cattolica del Sacro Cuore Rome Italy
1 shared publication - Elisa Di Fabio
Department of Biochemical Sciences “Alessandro Rossi Fanelli”, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy
1 shared publication
Latest Publications
- Open Access
- 10 June 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (12) , 6529
Immobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme’s performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid.
- 10 June 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (12) , 6529
Open AccessImmobilization of Lathyrus cicera Amine Oxidase on Magnetic Microparticles for Biocatalytic Applications
Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme’s performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid.